Thermodynamic Stability of Human Lens Recombinant αA- and αB-crystallins
Open Access
- 1 November 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (48) , 34067-34071
- https://doi.org/10.1074/jbc.274.48.34067
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- Detection and Characterization of α-Crystallin Intermediate with Maximal Chaperone-like ActivityBiochemical and Biophysical Research Communications, 1997
- Temperature‐induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α‐crystallinFEBS Letters, 1995
- Rapid Refolding Studies on the Chaperone-like α-CrystallinJournal of Biological Chemistry, 1995
- Dimerization of βB2‐crystallin: The role of the linker peptide and the N‐ and C‐terminal extensionsProtein Science, 1994
- Studies on the solubilization of the water-insoluble fraction from human lens and cataractExperimental Eye Research, 1992
- Alpha-crystallin can function as a molecular chaperone.Proceedings of the National Academy of Sciences, 1992
- Analysis of Protein Folding by Fast Protein Liquid Chromatography. Modular Domain Folding of γ-II-Crystallin from Calf Eye-LensBiological Chemistry Hoppe-Seyler, 1991
- Folding of an all-beta protein: independent domain folding in gamma II-crystallin from calf eye lens.Proceedings of the National Academy of Sciences, 1990
- Heat‐induced changes in the conformation of α‐ and β‐crystalline: Unique thermal stability of α‐crystallinFEBS Letters, 1988
- Short-range order of crystallin proteins accounts for eye lens transparencyNature, 1983